UniProt functional annotation for P08957



	UniProt functional annotation for P08957

UniProt code: P08957.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

Function: The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated. The EcoKI enzyme recognizes 5'-AACN(6)GTGC-3'.

Catalytic activity: Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L- homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA- COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;

Subunit: The type I restriction/modification system is composed of three polypeptides R, M and S.

Subunit: (Microbial infection) Interacts with Escherichia phage T7 protein Ocr; this interaction leads to the inhibition of the methyltransferase restriction enzyme M.EcoKI composed of M(2)S(1). {ECO:0000269|PubMed:12235377, ECO:0000269|PubMed:19074193}.

Miscellaneous: Type I restriction and modification enzymes are complex, multifunctional systems which require ATP, S-adenosyl methionine and Mg(2+) as cofactors and, in addition to their endonucleolytic and methylase activities, are potent DNA-dependent ATPases.

Similarity: Belongs to the N(4)/N(6)-methyltransferase family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



Function:		The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated. The EcoKI enzyme recognizes 5'-AACN(6)GTGC-3'.


Catalytic activity:		Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L- homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA- COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
Subunit:		The type I restriction/modification system is composed of three polypeptides R, M and S.
Subunit:		(Microbial infection) Interacts with Escherichia phage T7 protein Ocr; this interaction leads to the inhibition of the methyltransferase restriction enzyme M.EcoKI composed of M(2)S(1). {ECO:0000269\|PubMed:12235377, ECO:0000269\|PubMed:19074193}.
Miscellaneous:		Type I restriction and modification enzymes are complex, multifunctional systems which require ATP, S-adenosyl methionine and Mg(2+) as cofactors and, in addition to their endonucleolytic and methylase activities, are potent DNA-dependent ATPases.
Similarity:		Belongs to the N(4)/N(6)-methyltransferase family. {ECO:0000305}.